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7. sulfhydryl groups

All the individual steps are catalyzed by enzymes NAD" (Section 15 11) is required as an oxidizing agent and coenzyme A (Figure 26 16) is the acetyl group acceptor Coen zyme A is a thiol its chain terminates m a sulfhydryl (—SH) group Acetylation of the sulfhydryl group of coenzyme A gives acetyl coenzyme A... [Pg.1070]

We can descnbe the major elements of fatty acid biosynthesis by considering the for mation of butanoic acid from two molecules of acetyl coenzyme A The machinery responsible for accomplishing this conversion is a complex of enzymes known as fatty acid synthetase Certain portions of this complex referred to as acyl carrier protein (ACP), bear a side chain that is structurally similar to coenzyme A An important early step m fatty acid biosynthesis is the transfer of the acetyl group from a molecule of acetyl coenzyme A to the sulfhydryl group of acyl carrier protein... [Pg.1075]

Mode of Action. The fundamental biochemical lesion produced by arsenicals is the result of reaction between As " and the sulfhydryl groups of key respiratory enzymes such as pymvate and a-ketoglutarate dehydrogenases. [Pg.268]

Disulfides. As shown in Figure 4, the and h-chains of insulin are connected by two disulfide bridges and there is an intrachain cycHc disulfide link on the -chain (see Insulin and other antidiabetic drugs). Vasopressin [9034-50-8] and oxytocin [50-56-6] also contain disulfide links (48). Oxidation of thiols to disulfides and reduction of the latter back to thiols are quite common and important in biological systems, eg, cysteine to cystine or reduced Hpoic acid to oxidized Hpoic acid. Many enzymes depend on free SH groups for activation—deactivation reactions. The oxidation—reduction of glutathione (Glu-Cys-Gly) depends on the sulfhydryl group from cysteine. [Pg.379]

It is also possible to graft an aromatic amine antioxidant bearing a sulfhydryl group on to the backbone of an elastomer. [Pg.233]

As seen in Figure 1, the organo sulfur compounds are methylated at the boiling point (90°C) of dimethyl carbonate, whereas methylation (or alkylation with other alkyl groups) of other functional groups requites higher temperatures. This has resulted in the selective methylation of sulfhydryl groups of compounds that contain other substituents that can be alkylated. The other substituents can then be alkylated at elevated temperatures (63). [Pg.43]

This intermediate attacks compounds containing a variety of functional groups, such as primary, secondary, and tertiary amino nitrogen atoms, carboxyl groups, and sulfhydryl groups (10). [Pg.398]

Several mucolytics reduce the viscosity of mucus by cleaving the disulfide bonds that maintain the gel stmcture. AJ-Acet l-L-cysteine [616-91 -1] (19), introduced in 1963, and mesna [19677-45-5] (20), developed in Europe in the early 1970s (20,21), are effective compounds in this class. Whereas most mucolytics must be adrninistered by aerosol, carbocysteine [638-23-6] (21), which contains a derivatized sulfhydryl group, has shown activity by the oral route (22,23). However, carbocysteine does not reduce mucus viscosity, as does acetylcysteine, but appears to have a direct action on mucus glycoprotein production (24). [Pg.520]

Although a sulfhydryl group generally is not converted to an S-phenyl thioether, thiophenol can be used to introduce sulfur into molecules, and thus the phenyl group serves as a suitable protective group that can be removed by electrolysis (-2.7 V, DMF, R4N+X ). ... [Pg.288]

A thiol, usually under basic catalysis, can undergo Michael addition to an activated double bond, resulting in protection of the sulfhydryl group as a substituted 5-ethyl derivative. [Pg.295]

Displacement of the sulfhydryl group in primary thiols, like L cysteine and 2-diethylaminoethanethiol, requires elemental fluorine, the most active oxidant Elemental sulfur is the major by-product in those reactions [7] (equation 2)... [Pg.263]

Draw a simple mechanism for the reaction of a cysteine sulfhydryl group with iodoacetamide. [Pg.106]

The reason that Hb doesn t block the action of NO is due to a unique interaction between Cys93/3 of Hb and NO recently described by Li Jia, Celia and Joseph Bonaventura, andjohnathan Stamler at Duke University. Nitric oxide reacts with the sulfhydryl group of Cys93/3, forming an S-nitroso derivative ... [Pg.493]

The special properties of lipoic acid arise from the ring strain experienced by oxidized lipoic acid. The closed ring form is approximately 20 kj higher in energy than the open-chain form, and this results in a strong negative reduction potential of about —0.30 V. The oxidized form readily oxidizes cyanides to isothiocyanates and sulfhydryl groups to mixed disulfides. [Pg.601]

N02)2-C6H3K base. The sulfhydryl group in cysteine can be selectively protected in the presence of the amino group by reaction with 2,4-dinitrophenol at pH 5-6. ... [Pg.470]


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Acid phosphatase sulfhydryl groups

Albumin sulfhydryl groups

Alkylation of sulfhydryl group

Biotin sulfhydryl group

Blocking Sulfhydryl Groups

Blocking of the Sulfhydryl Group

Bonds and Sulfhydryl Groups

Cell division sulfhydryl group

Chemical modifications sulfhydryl groups

Chromatography sulfhydryl group

Dough sulfhydryl groups

Enalapril sulfhydryl group

Enzyme biological activity, sulfhydryl groups

Enzyme sulfhydryl groups

Epithelium, sulfhydryl group

Functional sulfhydryl groups

Hair, sulfhydryl group

Haptens with sulfhydryl groups

Insulin sulfhydryl groups

Metal ions sulfhydryl groups

Milk sulfhydryl groups

Molecular properties sulfhydryl groups

Muscle sulfhydryl groups

Phosphorylases sulfhydryl groups

Possible Interactions of Sulfhydryl Groups and Quinonoid Compounds

Protecting groups sulfhydryl

Protein sulfhydryl groups

Protein, acetylated sulfhydryl group

Succinic dehydrogenase sulfhydryl groups

Sucrose Sulfhydryl group

Sulfhydryl group coenzyme

Sulfhydryl group covalent modification

Sulfhydryl group of enzymes

Sulfhydryl group proton exchange

Sulfhydryl group, alkylation

Sulfhydryl group, analysis

Sulfhydryl groups , determination

Sulfhydryl groups Cystine

Sulfhydryl groups Replacement

Sulfhydryl groups Thiols

Sulfhydryl groups acetylation

Sulfhydryl groups activity

Sulfhydryl groups acylation

Sulfhydryl groups aminoethylation

Sulfhydryl groups amylases

Sulfhydryl groups and disulfide

Sulfhydryl groups and food safety

Sulfhydryl groups catalase

Sulfhydryl groups essential

Sulfhydryl groups esterases

Sulfhydryl groups ionization constants

Sulfhydryl groups masking

Sulfhydryl groups mercury

Sulfhydryl groups mercury exposure

Sulfhydryl groups modification

Sulfhydryl groups reactions

Sulfhydryl groups, amino acid

Sulfhydryl groups, amino acid structure

Sulfhydryl groups, cellular

Sulfhydryl groups, metal binding

Sulfhydryl groups, metal binding active site

Sulfhydryl groups, regulated

Sulfhydryls

Trace Elements and Sulfhydryl Groups

Use of Thiolation Reagents for Direct Labeling to Sulfhydryl Groups

Vitamin sulfhydryl group

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